Coagulation factor XIII serves as protein disulfide isomerase
| Autor: | Aida Inbal, Zsuzsa Bagoly, Eli Karniel, Rima Dardik, Judith Lahav, Vera Hazan Sheptovitsky |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
inorganic chemicals
RNase P Tissue transglutaminase Protein subunit Protein Renaturation Protein Disulfide-Isomerases Isomerase Klinikai orvostudományok Antibodies Bacitracin medicine Animals Humans Platelet Enzyme Inhibitors Protein disulfide-isomerase chemistry.chemical_classification Factor XIII biology Chemistry Orvostudományok Ribonuclease Pancreatic Hematology Molecular biology nervous system diseases body regions Protein Subunits Enzyme Biochemistry biology.protein Cattle Factor XIIIa medicine.drug |
| Zdroj: | Thrombosis and Haemostasis. 101:840-844 |
| ISSN: | 2567-689X 0340-6245 |
| Popis: | SummaryTissue transglutaminase was reported to act as protein disulfide isomerase (PDI). We studied whether plasma transglutaminase – coagulation factor XIII (FXIII) – has PDI activity as well. PDI activity was measured by determining the ability to renature reduced-denatured RNase (rdRNase). We found that FXIII can re-nature rdRNase, with efficiency comparable to commercial PDI. This PDI activity was inhibited by bacitracin. Like tissue transglu-taminase, FXIII-mediated PDI activity is independent of its transglutaminase activity and is located on the A subunit. Surface-associated PDI has been previously shown to catalyse two distinct functions: transnitrosation with subsequent release of intracellular nitric oxide and disulfide bond rearrangement during platelet integrin ligation. Our results imply that FXIII-PDI activity may have a role in platelet function. |
| Databáze: | OpenAIRE |
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